ArticleArchives of microbiology2025
Strategic targeting of AckA in Mycobacterium tuberculosis using peptide inhibitors.
Article in Archives of microbiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
1 citing paper in PubMed.
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Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Tuberculosis (TB) continues to pose a significant global health challenge, exacerbated by the rise of multidrug-resistant (MDR) and extensively drug-resistant (XDR) strains, which undermine the efficacy of existing therapies. Recent research focuses on anti-tubercular peptides as promising therapeutics due to their direct antimicrobial action and ability to enhance antibiotic efficacy by disrupting mycobacterial membranes. This study aims to identify and characterize potent anti-tubercular peptides targeting Acetate Kinase (AckA), a key enzyme in the metabolism of Mycobacterium tuberculosis. Through peptide virtual screening (PVS), followed by evaluations of cell penetration, toxicity, and MM/GBSA binding energy calculations, we identified five potential lead peptides, namely, DBAASP4864, DBAASP17881, DBAASP7096, DBAASP1043, and DBAASP5585, sourced from curated antimicrobial peptide databases (APD3, DBAASP, DRAMP, AntiTb, SATPdb, and CAMPR3). These candidates were selected based on favorable physicochemical properties, minimal toxicity, and strong binding affinities. Molecular dynamics simulations (MDS) demonstrated the structural stability of the peptide AckA complexes, with increased hydrogen bond formation observed over the simulation trajectories. Further validation through principal component analysis (PCA) and free energy landscape (FEL) mapping revealed a dominant low-energy basin, supporting the conformational stability of the complexes. MM/PBSA analysis confirmed strong binding interactions, and key residues, namely, Asn195, Asp266, Phe267, Gly314, and Asn318, were identified as critical contributors to peptide binding and complex stabilization. The study reveals peptide dynamics, highlighting their therapeutic potential and clinical applicability, while providing a strong foundation for experimental validation and developing next-generation anti-tubercular agents targeting drug-sensitive and drug-resistant M. tuberculosis strains.
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Identifiers
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.